Erythrocyte-binding antigen 175 mediates invasion in Plasmodium falciparum utilizing sialic acid-dependent and -independent pathways.
about
Plasmodium falciparum erythrocyte invasion: combining function with immune evasionInvasion by P. falciparum merozoites suggests a hierarchy of molecular interactionsIdentification and characterization of a novel Plasmodium falciparum adhesin involved in erythrocyte invasionIdentification and characterization of a novel Plasmodium falciparum merozoite apical protein involved in erythrocyte binding and invasionAntibodies to reticulocyte binding protein-like homologue 4 inhibit invasion of Plasmodium falciparum into human erythrocytesPlasmodium falciparum merozoite invasion is inhibited by antibodies that target the PfRh2a and b binding domainsDistinct external signals trigger sequential release of apical organelles during erythrocyte invasion by malaria parasitesStructural and Functional Basis for Inhibition of Erythrocyte Invasion by Antibodies that Target Plasmodium falciparum EBA-175Using mutagenesis and structural biology to map the binding site for the Plasmodium falciparum merozoite protein PfRh4 on the human immune adherence receptor.STEVOR is a Plasmodium falciparum erythrocyte binding protein that mediates merozoite invasion and rosettingTwo Plasmodium rhomboid proteases preferentially cleave different adhesins implicated in all invasive stages of malariaHuman erythrocyte band 3 functions as a receptor for the sialic acid-independent invasion of Plasmodium falciparum. Role of the RhopH3-MSP1 complexHost reticulocytes provide metabolic reservoirs that can be exploited by malaria parasitesDelineation of stage specific expression of Plasmodium falciparum EBA-175 by biologically functional region II monoclonal antibodiesPlasmodium falciparum merozoite surface protein 8 is a ring-stage membrane protein that localizes to the parasitophorous vacuole of infected erythrocytes.Intramembrane proteolysis mediates shedding of a key adhesin during erythrocyte invasion by the malaria parasitePlasmodium falciparum erythrocyte-binding antigen 175 triggers a biophysical change in the red blood cell that facilitates invasionComplement receptor 1 is the host erythrocyte receptor for Plasmodium falciparum PfRh4 invasion ligand.Systematic genetic analysis of the Plasmodium falciparum MSP7-like family reveals differences in protein expression, location, and importance in asexual growth of the blood-stage parasiteRH5-Basigin interaction plays a major role in the host tropism of Plasmodium falciparum.Plasmodium falciparum uses a key functional site in complement receptor type-1 for invasion of human erythrocytes.Molecular genetics and comparative genomics reveal RNAi is not functional in malaria parasites.Antibodies targeting the PfRH1 binding domain inhibit invasion of Plasmodium falciparum merozoitesA co-ligand complex anchors Plasmodium falciparum merozoites to the erythrocyte invasion receptor band 3.Acquisition of growth-inhibitory antibodies against blood-stage Plasmodium falciparum.Can prenatal malaria exposure produce an immune tolerant phenotype? A prospective birth cohort study in Kenya.Do apicomplexan parasite-encoded proteins act as both ligands and receptors during host cell invasion?Low-high season variation in Plasmodium falciparum erythrocyte binding antigen 175 (eba-175) allelic forms in malaria endemic area of Burkina Faso.PfCDPK1 mediated signaling in erythrocytic stages of Plasmodium falciparum.Changes in parasite virulence induced by the disruption of a single member of the 235 kDa rhoptry protein multigene family of Plasmodium yoelii.Evolution of human-chimpanzee differences in malaria susceptibility: relationship to human genetic loss of N-glycolylneuraminic acidEvaluation of three Pichia pastoris-expressed Plasmodium falciparum merozoite proteins as a combination vaccine against infection with blood-stage parasitesQuantitative proteomics reveals new insights into erythrocyte invasion by Plasmodium falciparumTransplacentally transferred functional antibodies against Plasmodium falciparum decrease with age.Targeting sialic acid dependent and independent pathways of invasion in Plasmodium falciparum.Identification of a specific region of Plasmodium falciparum EBL-1 that binds to host receptor glycophorin B and inhibits merozoite invasion in human red blood cellsCritical glycosylated residues in exon three of erythrocyte glycophorin A engage Plasmodium falciparum EBA-175 and define receptor specificity.Erythrocyte invasion receptors for Plasmodium falciparum: new and old.Subclass responses and their half-lives for antibodies against EBA175 and PfRh2 in naturally acquired immunity against Plasmodium falciparum malaria.Imbalanced distribution of Plasmodium falciparum EBA-175 genotypes related to clinical status in children from Bakoumba, Gabon.
P2860
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P2860
Erythrocyte-binding antigen 175 mediates invasion in Plasmodium falciparum utilizing sialic acid-dependent and -independent pathways.
description
2003 nî lūn-bûn
@nan
2003 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Erythrocyte-binding antigen 17 ...... ent and -independent pathways.
@ast
Erythrocyte-binding antigen 17 ...... ent and -independent pathways.
@en
Erythrocyte-binding antigen 17 ...... ent and -independent pathways.
@nl
type
label
Erythrocyte-binding antigen 17 ...... ent and -independent pathways.
@ast
Erythrocyte-binding antigen 17 ...... ent and -independent pathways.
@en
Erythrocyte-binding antigen 17 ...... ent and -independent pathways.
@nl
prefLabel
Erythrocyte-binding antigen 17 ...... ent and -independent pathways.
@ast
Erythrocyte-binding antigen 17 ...... ent and -independent pathways.
@en
Erythrocyte-binding antigen 17 ...... ent and -independent pathways.
@nl
P2860
P50
P356
P1476
Erythrocyte-binding antigen 17 ...... ent and -independent pathways.
@en
P2860
P304
P356
10.1073/PNAS.0730883100
P407
P577
2003-04-02T00:00:00Z